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Database: UniProt
Entry: Q9VE75_DROME
LinkDB: Q9VE75_DROME
Original site: Q9VE75_DROME 
ID   Q9VE75_DROME            Unreviewed;       834 AA.
AC   Q9VE75; Q9VE76; Q9XZ27;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 2.
DT   27-SEP-2017, entry version 143.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=Vha100-2 {ECO:0000313|EMBL:AAF55552.2,
GN   ECO:0000313|FlyBase:FBgn0028670};
GN   Synonyms=anon-WO0118547.296 {ECO:0000313|EMBL:AAF55552.2},
GN   BcDNA:LD21735 {ECO:0000313|EMBL:AAF55552.2}, Dmel\CG18617
GN   {ECO:0000313|EMBL:AAF55552.2}, vha100-2 {ECO:0000313|EMBL:AAF55552.2};
GN   ORFNames=CG18617 {ECO:0000313|EMBL:AAF55552.2,
GN   ECO:0000313|FlyBase:FBgn0028670}, CG7679
GN   {ECO:0000313|EMBL:AAF55552.2}, Dmel_CG18617
GN   {ECO:0000313|EMBL:AAF55552.2};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAD34771.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rubin G.M., Wan K.H., Harvey D., Lewis S.E., Brokstein P., Tsang G.,
RA   Agbayani A., Arcaina T.T., Baxter E., Blazej R.G., Butenhoff C.,
RA   Champe M., Chavez C., Chew M., Doyle C.M., Farfan D.E., Frise E.,
RA   Galle R., George R.A., Harris N.L., Hoskins R.A., Evans-Holm M.,
RA   Houston K.A., Hummasti S.R., Kim E., Li P., Moshrefi M., Pacleb J.M.,
RA   Park S., Sequeira A., Sethi H., Snir E., Svirskas R.R., Weinburg T.,
RA   Celniker S.E.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
RA   Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
RA   Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA   Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila
RT   melanogaster euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [4] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
RA   Ashburner M., Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin:
RT   a genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002).
RN   [6] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun
RT   assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [7] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [8] {ECO:0000313|EMBL:AAF55552.2}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
RA   Yu C., Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:AAF55552.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [11] {ECO:0000313|EMBL:AAF55552.2, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [12] {ECO:0000313|EMBL:AAF55552.2}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; AF132183; AAD34771.1; -; mRNA.
DR   EMBL; AE014297; AAF55551.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55552.2; -; Genomic_DNA.
DR   RefSeq; NP_650722.1; NM_142465.2.
DR   RefSeq; NP_732337.1; NM_169810.2.
DR   UniGene; Dm.3191; -.
DR   IntAct; Q9VE75; 14.
DR   MINT; MINT-835488; -.
DR   STRING; 7227.FBpp0083071; -.
DR   EnsemblMetazoa; FBtr0083656; FBpp0083071; FBgn0028670.
DR   EnsemblMetazoa; FBtr0083657; FBpp0083072; FBgn0028670.
DR   GeneID; 42216; -.
DR   KEGG; dme:Dmel_CG18617; -.
DR   UCSC; CG18617-RA; d. melanogaster.
DR   CTD; 42216; -.
DR   FlyBase; FBgn0028670; Vha100-2.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   GeneTree; ENSGT00390000004941; -.
DR   KO; K02154; -.
DR   OMA; FILRANH; -.
DR   OrthoDB; EOG091G01BI; -.
DR   ChiTaRS; Vha100-2; fly.
DR   GenomeRNAi; 42216; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0028670; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IMP:FlyBase.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:FlyBase.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISS:FlyBase.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; ISS:FlyBase.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000803};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Hydrolase {ECO:0000313|EMBL:AAF55552.2};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q9VE75};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    399    425       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    446    464       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    533    552       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    564    587       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    639    658       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    769    790       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       95    122       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   834 AA;  94849 MW;  21865E7DA535478A CRC64;
     MGDMFRSEEM ALCQMFIQPE AAYTSVSELG ETGCVQFRDL NVNVNAFQRK FVTEVRRCDE
     LERKIRYIET EIKKDGIVLP DIQDDIPRAP NPREIIDLEA HLEKTESEMI ELAQNEVNMK
     SNYLELTELR KVLENTQGFF SDQEVLNLDS SNRAGGDNDA AAQHRGRLGF VAGVINRERV
     FAFERMLWRI SRGNVFLKRS DLDEPLNDPA TGHPIYKTVF VAFFQGEQLK NRIKKVCTGF
     HASLYPCPSS HNEREEMVRN VRTRLEDLKL VLSQTEDHRS RVLATVSKNL PSWSIMVKKM
     KAIYHTLNLF NMDVTKKCLI GECWVPTNDL PVVQKALSDG SAAVGSTIPS FLNVIDTNEQ
     PPTFNRTNKF TRGFQNLIDA YGVASYRECN PALYTCITFP FLFAVMFGDL GHGLILVLFG
     AWMVLCERKL ARIRNGGEIW NIFFGGRYII LLMGLFAMYT GLVYNDVFSK SMNLFGSRWF
     NNYNTTTVLT NPNLQLPPNS SAVGVYPFGM DPVWQLADNK IIFLNSFKMK LSIIFGVLHM
     VFGVCMSVVN FTHFKRYASI FLEFVPQILF LLLLFGYMVF MMFFKWFSYN ARTSFQPETP
     GCAPSVLIMF INMMLFKNTE PPKGCNEFMF ESQPQLQKAF VLIALCCIPW MLLGKPLYIK
     FTRKNKAHAN HNGQLTGNIE LAEGETPLPT GFSGNEENAG GAHGHDDEPM SEIYIHQAIH
     TIEYVLSTIS HTASYLRLWA LSLAHAQLSE VLWQMVLSLG LKMSGVGGAI GLFIIFGAWC
     LFTLAILVLM EGLSAFLHTL RLHWVEFMSK FYEGMGYAFQ PFSFKAILDG EEEE
//
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